1lto

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[[Image:1lto.gif|left|200px]]
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{{STRUCTURE_1lto| PDB=1lto | SCENE= }}
{{STRUCTURE_1lto| PDB=1lto | SCENE= }}
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'''Human alpha1-tryptase'''
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===Human alpha1-tryptase===
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==Overview==
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Human mast cell tryptases represent a subfamily of trypsin-like serine proteinases implicated in asthma. Unlike beta-tryptases, alpha-tryptases apparently are proteolytically inactive. We have solved the 2.2A crystal structure of mature human alpha1-tryptase. It reveals a frame-like tetrameric architecture that, surprisingly, does not require heparin-binding for stability. In marked contrast to beta2-tryptase, the Ser214-Gly219 segment, which normally provides the template for substrate binding, is kinked in alpha-tryptase, thereby blocking its non-primed subsites. This so far unobserved subsite distortion is incompatible with productive substrate binding and processing. alpha-Tryptase apparently is trapped in this off-conformation by repulsions and attractions of the Asp216 side-chain. However, proteolytic activity could be generated by an induced-fit mechanism.
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(as it appears on PubMed at http://www.pubmed.gov), where 12162961 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12162961}}
==About this Structure==
==About this Structure==
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[[Category: Zettl, F.]]
[[Category: Zettl, F.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:16:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:12:17 2008''

Revision as of 19:12, 2 July 2008

Template:STRUCTURE 1lto

Human alpha1-tryptase

Template:ABSTRACT PUBMED 12162961

About this Structure

1LTO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of human alpha1-tryptase reveals a blocked substrate-binding region., Marquardt U, Zettl F, Huber R, Bode W, Sommerhoff C, J Mol Biol. 2002 Aug 16;321(3):491-502. PMID:12162961

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